Article
Recombinant proapoA-I(Lys107del) shows impaired lipid binding associated with reduced binding to plasma high density lipoprotein.
Atherosclerosis - 1 Nov 2001
Huang W, Matsunaga A, Li W, Han H, Hoang A, Kugi M, Koga T, Sviridov D, Fidge N, Sasaki J
Abstract excerpt
In the present study apoA-I (Lys 107del), a naturally occurring human apoA-I variant with a deletion of Lys 107, was expressed in E. coli to examine the effect of this mutation on lipid binding, cholesterol efflux and lecithin:cholesterol acyltranferase (LCAT) activation. Dimyristoyl phosphatidylcholine (DMPC) binding studies revealed slow interaction of proapoA-I(Lys107del) with DMPC relative to normal...
Topics
- Apolipoprotein A-I
- Apolipoproteins A
- Cells, Cultured
- Cholesterol
- Circular Dichroism
- Dimyristoylphosphatidylcholine
- Enzyme Activation
- Fibroblasts
- Humans
- Lipoproteins
- Lipoproteins, HDL
- Lysine
- Mutation
- Phosphatidylcholine-Sterol O-Acyltransferase